THE STRUCTURAL AND FUNCTIONAL BASIS OF ANTIBODY CATALYSIS

Author:

Wade Herschel1,Scanlan Thomas S.1

Affiliation:

1. The Departments of Pharmaceutical Chemistry and Cellular and Molecular Pharmacology, University of California, San Francisco, California 94143;

Abstract

▪ Abstract  Ten years have passed since the initial reports that antibodies could be programmed to have enzymatic activity by immunization with a transition-site analog. Much of the research over the last decade has focused on defining the scope and generality of antibody catalysis; however, during the past two years the first few crystal structures of catalytic antibody transition-state analogs have been reported. This review analyzes four such structures of catalytic antibodies that catalyze markedly different reactions, including ester hydrolysis, sulfide oxidation, and a pericyclic rearrangement. Structure-function relations for these catalysts are discussed and compared to the structure and function of natural enzymes, as well as the chemistry that occurs in solution.

Publisher

Annual Reviews

Subject

Structural Biology,Biophysics

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